• Journal of Microbiology and Biotechnology
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• v.13 no.5
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• pp.647-650
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• 2003

In anhydrous organic solvents, the complexes formed between AOT (dodecylbenzene sulfuric acid sodium salt) and hemoproteins, such as hemoglobin, myoglobin, or cytochrome c, displayed remarkably higher activity than the hemoprotein powders to oxidize dibenzothiophene, a model compound of organic sulfurs contained in fossil fuels. In slightly hydrophobic organic solvents, such as ethyl acetate and butyl acetate, dibenzothiophene was completely oxidized catalytically by the cytochrome c-AOT complex with cumene hydroperoxide (${\alpha},{\alpha}-dimethylbenzyl$ hydroperoxide) as an oxidant. In highly hydrophobic organic solvents, such as decane and hexadecane, however, the activity of the cytochrome c-AOT complex decreased, presumably due to the aggregation of the hemoprotein-AOT complex in these solvents.

• Analytical Science and Technology
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• v.8 no.2
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• pp.117-124
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• 1995

To Purify hemoproteins showing from 218nm absorbance, crude liver extract of human with hepatocirrhosis was treated with Triton N-101. Hemoproteins were purified by modification of Mohamed's method. This crude extract was applied to Octyl-Sepharose CL-4B column and the step elution was performed with 0.06% Lubrol PX and 0.25% Lubrol PX. The absorption of effluents were examined at 418nm and two peaks were appeared(Fig. 2). Hemoproteins were purified from Hyydroxyapatite and DEAE-Sephadex A-25 columns which the first peak was applied to(Fig. 3, 4). In death with suddenly, purified hemoproteins with 62 and 45kDa were obtained from 12.5% SDS-PAGE. In death with hepatocirrhosis, purified hemoprotein with 54kDa was obtainded from 12.5% SDS-PAGE(Fig. 5). Cytochrome P450 was purified to a specific content of 20.8nmol/mg protein with a recovery of about 4.1%. Absorbance maximum of these hemoproteins were 446nm at UV spectruum(Fig. 6).

• Journal of Microbiology and Biotechnology
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• v.17 no.12
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• pp.2066-2070
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• 2007

It was found that Shinorhizobium meliloti hemoprotein (SM) was more effective than Vitreoscilla hemoglobin (Vhb) in promoting secondary metabolites production when overexpressed in Streptomyces lividans TK24. The transformant with sm (sm-transformant) produced 2.7-times and 3-times larger amounts of actinorhodin than the vhb-transformant in solid culture and flask culture, respectively. In both solid and flask cultures, a larger amount of undecylprodigiocin was produced by the sm-transformant. It is considered that the overexpression of SM especially has activated the pentose phosphate pathway through oxidative stress, as evidenced by an increased NADPH production observed, and that it has promoted secondary metabolites biosynthesis.

• Biomolecules & Therapeutics
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• v.22 no.6
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• pp.491-496
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• 2014

Photobiomodulation utilizes monochromatic (or quasimonochromatic) light in the electromagnetic region of 600~1000 nm for the treatment of soft tissues in a nondestructive and nonthermal mode. It is conceivable that photobiomodulation is based upon the ability of the light to alter cell metabolism as it is absorbed by general hemoproteins and cytochrome c oxidase (COX) in particular. Recently it has been suggested radiation of visible and infrared (IR) activates retrograde signaling pathway from mitochondria to nucleus. In this review, the role of COX in the photobiomodulation will be discussed. Further a possible role of water as a photoreceptor will be suggested.

• Microbiology and Biotechnology Letters
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• v.24 no.5
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• pp.579-584
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• 1996

The molecular weight of the purified nucleoside oxidase estimated by gel filtration column chromatography was 480,000 and the enzyme protein was composed of four nonidentical subunits (81,000, 69,000, 32,000 and 16,000). On the basis of the visible absorption spectra and the enzymatic determination of the purified enzyme, the enzyme was supposed as a hemoprotein and also a flavoprotein containing 3 moles of FAD per I mole of enzyme. The isoelectric point of the enzyme was pH 5.1. Addition of metal salts such as 1 mM SnCl$_{2}$ and PbCl$_{2}$ into an enzyme reaction solution inhibited the enzyme activity by 94 and 90%, respectively. The enzyme activity was also lost significantly by hemoenzyme inhibitors such as NaCN and NaN$_{3}$ and flavoenzyme inhibitor, acriflavine and quinacrine. The maximal nucleoside oxidase activity was observed at pH 7.0 and 55$\circ$C. The nucleoside oxidase was relatively stable in the range of pH 5.5-9.0 and below 55$\circ$C.

• YAKHAK HOEJI
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• v.32 no.6
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• pp.420-427
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• 1988

Post-translational modification of protein amino acid residues is a well known metabolic phenomenon. One such side chain modification, protein methylation, occur ubiquitously in nature, in organism ranging from prokaryotic to eukaryotic and the biological significance of protein methylation has begun to emerge. The observation that cytochrome C methylation facilitates the binding of this hemoprotein to mitochondria could be placed as the one of the examples along this line. However, the detail biological meaning of cytochrome C methylation is remained to be clarified. In the aspect of such reason this research was done. The results of this experiment were; 1) pure Euglena gracilis cytochrome C552 was isolated, 2) methylarginine and methylmethionine were not found in cytochrome C552 sequence, 3) however, Unknown Peak at 20.78min of retention time was found, and 4) this Unknown Peak was found only from Euglena cytochrome C552, so far.

• Microbiology and Biotechnology Letters
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• v.24 no.5
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• pp.585-590
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• 1996

Peroxidase was purified to homogeneity from cell free extract of Flavobacterium meningosepticum. The molecular weight of the enzyme estimated by gel filtration column chromatography was 220, 000. A identical subunit (54, 000) was detected on SDS-PAGE of the enzyme. From these results, the enzyme was supposed to have four identical subunits. On the basis of the visible absorption spectra of the purified enzyme, the enzyme was a typical hemoprotein. The isoelectric point of the enzyme was 4.1. On using N-ethyl-N-(2-hydroxy-3-sulfopropyl)-m- toluidine (Toos) as a hydrogen donor, the enzyme showed optimum activity at the pH 5.5 and 50$\circ$C. The enzyme activity was inhibited by carbonyl reagent and Hg$^{2+}$ .

• Archives of Pharmacal Research
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• v.21 no.3
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• pp.305-309
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• 1998

Human cytochrome P450 1A2 is one of the major cytochrome P450s in human liver. It is known to be capable of activating a number of carcinogens such as arylamines and heterocyclic amines. In order to develop the new bacterial mutagenicity test system with human P450, a full length of human P450 1A2 cDNA inserted into pCW bacterial expression vector was introduced to Escherichia coli WP2 uvrA strain which is a well-known E. coli strain for bacterial reverse mutagenicity assay. Expressed human P450 1A2 showed typical P450 hemoprotein spectra. Maximum expression was achieved at 48 hrs after incubating at $30^{\circ}C$ in terrific broth containing ampicillin, IPTG and other supplements. High level expression of P450 1A2 in E. coli WP2 uvrA membranes was determined in SDS-PAGE. The well-known mutagens 2-aminoanthracene and MElQ increased the revertant colonies of E. coli WP2 uvrA expressing human P450 1A2 without an exogenous rat hepatic post-mitochondrial supernatant (S9 fraction) in a dose-dependent manner. The results show that the functional expression of human P450 in bacterial mutagenicity tester strain will provide a useful tool for studying the mechanism of the mutagenesis and carcinogenesis of new drugs and environmental chemicals.

• Analytical Science and Technology
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• v.11 no.1
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• pp.73-78
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• 1998

The reverse detection heteronuclear multiple quantum coherence, HMQC study of metcyano complex of horse myoglobin(MbCN) has provided the complete assignment of hyperfine shifted resonances of heme carbons attached with proton(s). The application of HMQC experiment to the paramagnetic low-spin MbCN gives clear $^1H$ and $^{13}C$ coherences for the paramagnetic amino acid residues as well as heme side chains, and can be extended to the low-spin paramagnetic hemoprotein derivative for the assignment of natural abundance $^{13}C$ resonances. This assignment strategy can avoid possible ambiguities that may result from the sole utilization of $^1H$ nuclear Overhauser effect for the assignment of heme $^1H$ signals resonating in the diamagnetic region. The resulting 2,4-vinyl ${\alpha}$-carbons and 7-propionate ${\beta}$-carbon follow anomalous anti-Curie behavior, and are indicative of incoplanarity with heme plane. Magnetic/electronic asymmetry of heme induced by proximal histidine(His) makes spread that the hyperfine shifted heme carbon resonances over the range of 250 ppm at $25^{\circ}C$. These heme carbon resonances would be the much more sensitive probe than those of proton resonances in analyzing the nature of heme electronic structure of myoglobin.